ID A0A165FMJ0_XYLHT Unreviewed; 591 AA.
AC A0A165FMJ0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS00028};
GN ORFNames=L228DRAFT_248930 {ECO:0000313|EMBL:KZF21158.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF21158.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF21158.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF21158.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the REI1 family.
CC {ECO:0000256|ARBA:ARBA00034126}.
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DR EMBL; KV407461; KZF21158.1; -; Genomic_DNA.
DR RefSeq; XP_018186713.1; XM_018332975.1.
DR AlphaFoldDB; A0A165FMJ0; -.
DR STRING; 1328760.A0A165FMJ0; -.
DR GeneID; 28898112; -.
DR InParanoid; A0A165FMJ0; -.
DR OMA; NATHMER; -.
DR OrthoDB; 180831at2759; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040025; Znf622/Rei1/Reh1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13182; ZINC FINGER PROTEIN 622; 1.
DR PANTHER; PTHR13182:SF8; ZINC FINGER PROTEIN 622; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..37
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT DOMAIN 80..102
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 103..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 66056 MW; 3F9AB91DE244E89E CRC64;
MSARANVAQS HPFTCNTCQV AFRSSELQRG HMHSDWHRYN LKRRVASLPP LASEAFAEKV
LSAQASTTAA AAKAAFEKSC DACQKTYYSE NAYANHLGSQ KHRANASALK NRPATNKQDD
ETQSVMSSTF SLGEPVEVGS TIEETPAAEK EFSNVVDSLK NATINDKEPI SRRPTRPHHS
SQDARPEHPL SQTTTETEKA DNEDEDADGE ETEESVPLSK CLFCNLESPS LDVNVTHMSK
NHGMFIPERP FLVDLAGLVS YLYEKIADLH ECLYCGKFKS TAEGVQTHMR DKGHCMIAYS
TEQEMLEIGQ FYDFRGTYSD EESEEDSESY DSEEEDEEWE SADEDEEDED LARSPGGGVK
LGAKRDAHTK TMLTTEDGAE QEVASGAEEG EGWETDSDAS SVASDEITAI PVDVYPRREK
LVKHRHHSHH DPRPHRNADG WHSRAHTTPR AVYHDDFELH LPSGRTAGHR SLAKYYRQNL
RNYPTPEERA NQQAIAEDAH VSSDDERGAG IDGEGRGREL QQRGGRDRGR QIISRANGGT
GMLGVTDGKK KEVSATEKRE TKRGQRAQAR YQWGVEKRGN HQKHFRDPLL Q
//
